2pse: Difference between revisions
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==Overview== | ==Overview== | ||
Due to its ability to emit light, the luciferase from Renilla reniformis | Due to its ability to emit light, the luciferase from Renilla reniformis (RLuc) is widely employed in molecular biology as a reporter gene in cell culture experiments and small animal imaging. To accomplish this bioluminescence, the 37-kDa enzyme catalyzes the degradation of its substrate coelenterazine in the presence of molecular oxygen, resulting in the product coelenteramide, carbon dioxide, and the desired photon of light. We successfully crystallized a stabilized variant of this important protein (RLuc8) and herein present the first structures for any coelenterazine-using luciferase. These structures are based on high-resolution data measured to 1.4 A and demonstrate a classic alpha/beta-hydrolase fold. We also present data of a coelenteramide-bound luciferase and reason that this structure represents a secondary conformational form following shift of the product out of the primary active site. During the course of this work, the structure of the luciferase's accessory green fluorescent protein (RrGFP) was also determined and shown to be highly similar to that of Aequorea victoria GFP. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Renilla-luciferin 2-monooxygenase]] | [[Category: Renilla-luciferin 2-monooxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fenn, T | [[Category: Fenn, T D.]] | ||
[[Category: Gambhir, S | [[Category: Gambhir, S S.]] | ||
[[Category: Loening, A | [[Category: Loening, A M.]] | ||
[[Category: IMD]] | [[Category: IMD]] | ||
[[Category: alpha/beta-hydrolase]] | [[Category: alpha/beta-hydrolase]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:31 2008'' | ||
Revision as of 19:32, 21 February 2008
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Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis
OverviewOverview
Due to its ability to emit light, the luciferase from Renilla reniformis (RLuc) is widely employed in molecular biology as a reporter gene in cell culture experiments and small animal imaging. To accomplish this bioluminescence, the 37-kDa enzyme catalyzes the degradation of its substrate coelenterazine in the presence of molecular oxygen, resulting in the product coelenteramide, carbon dioxide, and the desired photon of light. We successfully crystallized a stabilized variant of this important protein (RLuc8) and herein present the first structures for any coelenterazine-using luciferase. These structures are based on high-resolution data measured to 1.4 A and demonstrate a classic alpha/beta-hydrolase fold. We also present data of a coelenteramide-bound luciferase and reason that this structure represents a secondary conformational form following shift of the product out of the primary active site. During the course of this work, the structure of the luciferase's accessory green fluorescent protein (RrGFP) was also determined and shown to be highly similar to that of Aequorea victoria GFP.
About this StructureAbout this Structure
2PSE is a Single protein structure of sequence from Renilla reniformis with as ligand. Active as Renilla-luciferin 2-monooxygenase, with EC number 1.13.12.5 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis., Loening AM, Fenn TD, Gambhir SS, J Mol Biol. 2007 Dec 7;374(4):1017-28. Epub 2007 Oct 3. PMID:17980388
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